The role of cysteine residues in the transport of mercuric ions by the Tn501 MerT and MerP mercury-resistance proteins.

doi:10.1111/j.1365-2958.1995.mmi_17010025.x

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Article

The role of cysteine residues in the transport of mercuric ions by the Tn501 MerT and MerP mercury-resistance proteins.

Molecular microbiology - 1 Jul 1995

Morby A P, Hobman J L, Brown N L

Abstract excerpt

Each cysteine residue in the MerT and MerP polypeptides of bacterial transposon Tn501 was replaced by serine, and the mercury-resistance phenotypes of the mutants were determined in Escherichia coli. Cys-24 and Cys-25 in the first transmembrane region of MerT were essential for transport of mercuric ions through the cytoplasmic membrane, and mutations Cys-76-Ser, Cys-82-Ser or Gly-38-Asp in MerT or Cys-36-Ser in...

Topics

Amino Acid Sequence
Bacterial Proteins
Base Sequence
Carrier Proteins
Cation Transport Proteins
Cell Membrane
Cysteine
Cytoplasm
DNA Transposable Elements
Drug Resistance, Microbial
Escherichia coli

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Ion Transport

Membrane Proteins

Mercuric Chloride

Molecular Sequence Data

Mutation

Operon

Oxidoreductases

Source

Open in PubMed

Identifiers

PMID: 7476206
DOI: 10.1111/j.1365-2958.1995.mmi_17010025.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7476206-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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The role of cysteine residues in the transport of mercuric ions by the Tn501 MerT and MerP mercury-resistance proteins.PMID 7476206Read ↗

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Mutations in dsbA and dsbB, but not dsbC, lead to an enhanced sensitivity of Escherichia coli to Hg2+ and Cd2+.Semantic proximity Read ↗

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